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Biomedical subjects

Z Deyl

Publications and source records attributed to Z Deyl.

At least 91 records · Page 5Linked to original sources
PubMed1985

Drug level monitoring: chromatography of some minor groups of drugs.

Some important facts about the chromatographic separation of a number of selected categories of drugs are summarized. The data refer to the chromatographic method of choice, stationary phase, mobile phase (carrier gas), detection procedure and (where available) method sensitivity. Also, fundamental instrumental parameters, namely injector, column and detector temperature, carrier gas and mobile phase flow-rate and gradient set-up are reported here. In all cases also the source material used for analysis is specified. The data are presented in table form, each table dealing with a particular category of drugs. The following categories of drugs are being dealt with: anthelmintics, antiarteriosclerotics, antibacterials, anticholinergics and cholinergics, anticoagulants, antidiabetics, antiemetics, antimycotics, antihistamines, antimalarials, antiparasitics, antiparkinsonics, antitussives, antiulcer drugs, antiviral compounds, appetite depressants and immunosuppressives.

Anthelmintics↗
PubMed1985

Changes in glomerular basement membrane collagen caused by DOCA-NaCl treatment in rats.

The influence of hypertensive regime on collagen synthesis in glomerular basement membranes of rats was studied. Isolated glomeruli were incubated in a medium containing 14C-labeled proline. It was demonstrated that there was a higher proline incorporation and proline conversion to hydroxyproline in rats kept on the hypertensive regime. However, solubilization of the collagenous fraction by limited pepsin digestion did not reveal any qualitative changes in the collagen type deposited. It is concluded that the DOCA-NaCl treatment in rats results in an intensive accumulation of collagen, mainly of type IV, typical for basement membranes.

Animals↗
PubMed1984

Degenerated annulus fibrosus of the intervertebral disc contains collagen type II.

Collagen has been isolated and purified from the pronase digest of the outer annulus fibrosus of degenerated and unaffected intervertebral discs obtained at necropsy. The mixture of different collagen types has been purified and fractionated by 2 subsequent DEAE-cellulose chromatographic procedures according to established methods. Collagen chain polymers were then isolated by molecular sieving. Their reduction with 2-mercaptoethanol followed by agarose chromatography resulted in the separation of 3 major peaks corresponding to gamma, beta, and alpha chains. Cyanogen bromide (CNBr) peptides and aminoacid analyses revealed the identity of the isolated alpha-chain as alpha 1(III). Further support for this finding was obtained by immunofluorescence. It is suggested that the presence of collagen type III in the outer annulus fibrosus may be related to intervertebral disc prolapse.

Aged↗
PubMed1984

Changes in collagen metabolism--another look at osteoarthrosis.

Collagen types I and III were isolated from osteoarthrotic cartilage. Immunofluorescence study has shown that these two collagen types are present in the deep layers of cartilage. Additional staining for fibronectin revealed the presence of the cell-adhesive protein in osteoarthrotic cartilage. Neither collagen type I and type III nor fibronectin were found in control cartilage. A passive haemagglutination assay determined anticollagen antibodies (against types I, II and III) in sera of some osteoarthrotic patients.

Cartilage, Articular↗
PubMed1984

Age dependence of the gamma-carboxyglutamic acid containing proteins.

A distinct age dependence was observed in the occurrence of the gamma-carboxyglutamic acid containing proteins obtained from kidney cortex, liver and femoral bone. In the femoral bone, a stepped increase was seen when comparing animals 60, 350 and 700 days old. In the liver and mainly in the kidney cortex there was no change during the first year of life, but a distinct increase in the gamma-carboxyglutamate containing proteins was seen between day 350 and 700. It was also established that the increased level of gamma-carboxyglutamate at least in kidney cortex is due to a more intense carboxylation reaction in older animals as increased incorporation of labelled bicarbonate was observed in the microsomal fraction. In accordance with our previous results the occurrence of the carboxyglutamic acid containing proteins was shown to be vitamin D dependent; in vitamin D deprived animals supplemented with this vitamin the reappearance of gamma-carboxylate is more distinct in situations where higher levels of gamma-carboxyglutamic acid occur physiologically.

1-Carboxyglutamic Acid↗
PubMed1983

Altered expression of collagen phenotype in osteoarthrosis.

Immunofluorescence studies have shown the presence of collagen type III in addition to types I and II in osteoarthrotic cartilage. The presence of collagen type III was verified biochemically: collagen was isolated and purified from the pronase digest of osteoarthrotic cartilage. Mixtures of different collagen types were fractionated first by two different DEAE-cellulose runs and then the collagen polymers were isolated by molecular sieve chromatography. Afterwards the collagenous material was reduced, Alkylated, and rechromatographed on an agarose column. Three major peaks corresponding to gamma-, beta- and alpha-chains were observed. Amino acid analyses and the CNBr peptide pattern indicated the identity of the alpha peak as alpha 1 (III). Additional staining of control and disease cartilages for fibronectin revealed the presence of this protein in the diseased tissue.

Bone Diseases↗
PubMed1983

Evidence for vitamin D dependent gamma-carboxylation in osteocalcin related proteins.

The content of gamma-carboxyglutamic acid (gla) was determined in rat femoral bone and kidney cortex in rachitic and vitamin D treated animals. It was demonstrated that the level of gla is decreased in vitamin D depleted animals both in kidney cortex and femoral bone. Supplementation of vitamin D deprived animals with this vitamin resulted in an increase in the gla concentration to almost normal levels. Also the incorporation of 14C NaHCO3 in renal cortex microsomes from rachitic animals was blocked. It is suggested that the absence of gla resulted from the direct action of vitamin D on mRNA for the Ca-binding protein.

1-Carboxyglutamic Acid↗
PubMed1983

Fibronectin is not a serum spreading factor for HeLa cells.

The spreading of HeLa cells on plastic substratum is mediated by fibronectin-depleted foetal calf serum but not by fibronectin isolated by gelatin-Sepharose affinity chromatography. The same is true for freshly explanted chick embryonic chondrocytes. In contrast, BHK cell spreading exceeds 67% after 120 min at 37 degrees C in fibronectin-supplemented (10 micrograms ml-1) serum-free medium. Long-term cultivation of HeLa cells in Eagle's MEM supplemented with fibronectin-free serum is associated with the accumulation of cells in mitosis or before cytokinesis; many cells die and the remaining living cells, characterized by marked changes in morphology, multiply very slowly. It can be concluded therefore that fibronectin does not produce spreading in HeLa cells but forces them into mitosis.

Animals↗
PubMed1983

Are the changes in collagen caused by chronical X-irradiation similar to aging?

It has been shown that in the skin of chronically irradiated rats the proportion of collagen type III as compared to collagen type I is increased; on the other hand, no changes in the overall proportion to collagen were observed in the skin. It appears that the increased proportion of collagen type III in chronically irradiated rats is responsible for the decreased solubility of cutaneous collagen in these animals. Concomitantly, indirect evidence was accumulated for the presence of an additional cross-link in type III collagen, present only when irradiated animals served as the collagen source. This cross-link is located subterminally as long as it is not removed by limited pepsin digestion. It was concluded that the physiological decrease in solubility and the decrease in solubility observed in chronically irradiated animals have a different molecular background.

Aging↗
PubMed1983

Changes in serum and tissue fibronectin during ontogeny.

It has been proved that both in bovine and rat serum fibronectin concentration increases with age. While in foetal bovine the serum fibronectin concentration was 77 +/- 5 micrograms/ml, in adult cows the concentration of this protein reached 150.0 +/- 5.5 micrograms/ml. In newborn rats, the corresponding fibronectin concentration in the serum was 227 +/- 25 micrograms/ml as compared to 455 +/- 47 micrograms/ml in adult individuals. On the contrary, a drop in fibronectin concentration was found in the bovine glomerular basement membrane: fibronectin represents 3.8 +/- 0.6% of total protein in the newborn, while in animals older than two months this protein was not detectable. Accordingly, in newborn rats fibronectin represents 5.1 +/- 0.6% of total protein in the glomerular basement membrane and drops dramatically to 0.4 +/- 0.1% after one year of life with no detectable changes thereafter. In the alveolar basement membrane the changes are similar as in the glomerular basement membrane. While in newborn rats this protein represents 13.2 +/- 0.5% of total basement membrane protein, it drops to 3.2 +/- 0.3% after two years of life.

Aging↗
PubMed1982

The role of oxidative cross-link stabilization in increased collagen polymerization in food deprived rats.

It was demonstrated that 50% food restriction for a period of two years causes a considerable increase in gamma-chain polymers of rat skin collagen. The polymerization reaction occurs in both main skin collagen types, e.g. collagen type I and III. Concomitantly increased amounts of alpha-aminoadipic acid were found in preparations of food deprived rats as compared to the controls. It appears that this unusual amino acid arises from the oxidative stabilization of dehydro hydroxylysinonorleucine, the main intermolecular collagen cross-link present in the skin. It is suggested that the degree of polymerization of skin collagen in fasted animals is the result of reutilization of more soluble collagen forms.

2-Aminoadipic Acid↗
PubMed1982

Decrease in pyrrole-2-carboxylic acid excretion during lung cancer disease.

A statistically significant decrease of pyrrole-2-carboxylic acid in urine was observed in lung cancer of stage I (TNM classification) when compared to that of healthy miners (chronically exposed to radiation) from the uranium industry. The difference vanishes in stage II of the disease and reappears in stage III. While nonmalignant lung diseases (bronchopneumonia and chronic bronchitis) do not interfer in the stage I with the drop of pyrrole-2-carboxylic acid excretion, in stage III of lung cancer the decrease is less pronounced and cannot be differentiated from that found in bronchopneumonia or chronic bronchitis.

Collagen↗